TY - JOUR ID - 103900 TI - Two-step purification and partial characterization of an extra cellular α-amylase from Bacillus licheniformis JO - Archives of Razi Institute JA - ARI LA - en SN - 0365-3439 AU - Zare Mirakabadi, A. AU - Ghorbanpour, M. AU - Sadeghi, A. AU - Sarzaeem, A. AD - Department of venomous animals and anti venom production, Razi Vaccine & Serum Research Institute, Karaj, Iran AD - Department of Chemical Engineering, Amirkabir University, Tehran, Iran Y1 - 2012 PY - 2012 VL - 67 IS - 2 SP - 155 EP - 160 KW - α KW - amylase KW - Bacillus licheniformis KW - optimal conditions KW - PURIFICATION DO - 10.22092/ari.2016.103900 N2 - The aim of this study was production and partial purification of α-amylase enzyme by Bacillus licheniformis. B. Licheniformis was allowed to grow in broth culture for purpose of inducing α-amylase enzyme. Optimal conditions for amylase production by B. Licheniformis are incubation period of 120 h, temperature of 37 °C and pH 7.0. The α-amylase enzyme was purified by ion exchange chromatography on DEAE-sepharose CL-6B and sephadex G-100 gel filtration with a 19.1-fold increase in specific activity as compared to the concentrated supernatant and with a specific activity of 926.47 U/mg. The α-amylase had the highest activity at pH 7.0 and 65 °C. According to the data on native polyacrylamide gel electrophoresis, the molecular weight of the purified enzyme was 72 kDa. UR - https://archrazi.areeo.ac.ir/article_103900.html L1 - https://archrazi.areeo.ac.ir/article_103900_20c251f32823f6c382e5c51451486b5a.pdf ER -